Crystal structure of Negative Cofactor 2 recognizing the TBP-DNA transcription complex

  • Kamada K
  • Shu F
  • Chen H
 et al. 
  • 47

    Readers

    Mendeley users who have this article in their library.
  • 106

    Citations

    Citations of this article.

Abstract

The X-ray structure of a ternary complex of Negative Cofactor 2 (NC2), the TATA box binding protein (TBP), and DNA has been determined at 2.6 Å resolution. The N termini of NC2 α and β resemble histones H2A and H2B, respectively, and form a heterodimer that binds to the bent DNA double helix on the underside of the preformed TBP-DNA complex via electrostatic interactions. NC2β contributes to inhibition of TATA-dependent transcription through interactions of its C-terminal α helix with a conserved hydrophobic feature on the upper surface of TBP, which in turn positions the penultimate α helix of NC2β to block recognition of the TBP-DNA complex by transcription factor IIB. Further regulatory implications of the NC2 heterodimer structure are discussed.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

  • Katsuhiko Kamada

  • Fong Shu

  • Hua Chen

  • Sohail Malik

  • Gertraud Stelzer

  • Robert G. Roeder

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free